Biomolecules. Protein Carbohydrate Nucleic acid Lipid
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1 01. Amino Acids 1
2 Biomolecules Protein Carbohydrate Nucleic acid Lipid 2
3 peptide polypeptide protein di-, tri-, oligo- 3
4 4
5 fibrous proteins proteins globular proteins 5
6 Figure 4.1 Anatomy of an amino acid. Except for proline and its derivatives, all of the amino acids commonly found in proteins possess this type of structure. 6
7 Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V)* Leucine (Leu, L)* Isoleucine (Ile. I)* 7
8 Serine (Ser, S) Threonine (Thr, T)* Cysteine (Cys, C) cystine Methionine (Met, M)* 8
9 Aspartate (Asp, D) Glutamate (Glu, E) Asparagine (Asn, N) Glutamine (Gln, Q) 9
10 Lysine (Lys, K)* Arginine (Arg, R)* 10
11 Phenylalanine (Phe, F)* Tyrosine (Tyr, Y) Histidine (His, H)* Tryptophan (Trp, W)* 11
12 Proline (Pro, P) 12
13 Hydrophobic (A, G, I, L, F, V, P) Hydrophilic (D, E, R, S, T, C, N, Q, H) Amphipathic (K, M, W, Y) 13
14 Essential amino acids: V, L, I, T, M, K, R, F, H, W 14
15 Several Amino Acids Occur Rarely in Proteins We'll see some of these in later chapters Selenocysteine in many organisms Pyrrolysine in several archaeal species Hydroxylysine, hydroxyproline - collagen Carboxyglutamate - blood-clotting proteins Pyroglutamate in bacteriorhodopsin GABA, epinephrine, histamine, serotonin act as neurotransmitters and hormones Phosphorylated amino acids a signaling device
16 Several Amino Acids Occur Rarely in Proteins
17 Several Amino Acids Occur Rarely in Proteins Figure 4.4 (b) Some amino acids are less common, but nevertheless found in certain proteins. Hydroxylysine and hydroxyproline are found in connective-tissue proteins; carboxyglutamate is found in blood-clotting proteins; pyroglutamate is found in bacteriorhodopsin (see Chapter 9).
18 Several Amino Acids Occur Rarely in Proteins Figure 4.4 (c) Several amino acids that act as neurotransmitters and hormones.
19 Stereochemistry of Amino Acids 19
20 20
21 The Murchison Meteorite Discovery of Extraterrestrial Handedness Why do L-amino acids predominate in biological systems? What process might have selected L-amino acids over their D- counterparts? The meteorite found near Murchison, Australia may provide answers. Certain amino acids found in the meteorite have been found to have L-enantiomeric excesses of 2% to 9%.
22 Which is (2S,3R)-threonine? 22
23 4.2 What Are Acid-Base Properties of Amino Acids? Amino Acids are Weak Polyprotic Acids The degree of dissociation depends on the ph of the medium H 2 A + + H 2 O HA 0 + H 3 O + K a1 = 0 [ HA ][ H 0 ] [ HA] +
24 4.2 What Are Acid-Base Properties of Amino Acids? The second dissociation (the amino group in the case of glycine): HA 0 + H 2 O A + H 3 O + K A HO + = 3 a2 0 [ ][ ] [ HA ]
25 4.2 What Are Acid-Base Properties of Amino Acids? Figure 4.5 The ionic forms of the amino acids, shown without consideration of any ionizations on the side chain.
26 The adjacent α-amino group makes the α-cooh group more acidic. 26
27 4.2 What Are Acid-Base Properties of Amino Acids?
28 pk a Values of the Amino Acids You should know these numbers and know what they mean Alpha carboxyl group - pk a = 2 Alpha amino group - pk a = 9 These numbers are approximate, but entirely suitable for our purposes.
29 29
30 Protonated at physiological ph 30
31 pka =
32 32
33 pk a Values of the Amino Acids You should know these numbers and know what they mean Arginine, Arg, R: pk a (guanidino group) = 12.5 Aspartic Acid, Asp, D: pk a = 3.9 Cysteine, Cys, C: pk a = 8.3 Glutamic Acid, Glu, E: pk a = 4.3 Histidine, His, H: pk a = 6.0
34 pk a Values of the Amino Acids You should know these numbers and know what they mean Lysine, Lys, K: pk a = 10.5 Serine, Ser, S: pk a = 13 Threonine, Thr, T: pk a = 13 Tyrosine, Tyr, Y: pk a = 10.1
35 Another Sample Calculation What is the ph of a lysine solution if the side chain amino group is 3/4 dissociated? ph = log 10 [1] ph = (0.477) ph = = 11.0 [3] Note that, when the group is ¾ dissociated, ¾ is dissociated and ¼ is not; thus the ratio in the log term is ¾ over ¼ or 3/1. OC p60 Henderson-Hasselbalch eq
36 K a = [H 3 O + ][A - ] [HA] = K eq [H 2 O] pk a = -log K a If ph < pk a, acidic form If ph > pka, basic form See p60 36
37 Isoelectric point (IP): no net charge 37
38 38
39 Reactions of Amino Acids Carboxyl groups form amides & esters Amino groups form Schiff bases and amides Edman reagent (phenylisothiocyanate) reacts with the α-amino group of an amino acid or peptide to produce a phenylthiohydantoin (PTH) derivative. Side chains show unique reactivities Cys residues can form disulfides and can be easily alkylated Few reactions are specific to a single kind of side chain
40 Green Fluorescent Protein A jellyfish (Aequorea victoria) native to the northwest Pacific Ocean contains a green fluorescent protein. GFP is a naturally fluorescent protein. Genetic engineering techniques can be used to tag virtually any protein, structure, or organelle in a cell. The GFP chromophore lies in the center of a β-barrel protein structure.
41 Green Fluorescent Protein The prosthetic group of GFP is an oxidative product of the sequence FSYGVQ-.
42 Yellow fluorescent protein Amino acid substitutions in GFP can tune the color of emitted light. Shown here is an image of African green monkey kidney cells expressing yellow fluorescent protein (YFP) fused to α- tubulin, a cytoskeletal protein.
43 Spectroscopic Properties All amino acids absorb at infrared wavelengths Only Phe, Tyr, and Trp absorb UV Absorbance at 280 nm is a good diagnostic device for amino acids NMR spectra are characteristic of each residue in a protein, and high resolution NMR measurements can be used to elucidate three-dimensional structures of proteins
44 Spectroscopic Properties Figure 4.10 The UV spectra of the aromatic amino acids at ph 6.
45 Spectroscopic Properties Figure 4.11 Proton NMR spectra of several amino acids.
46 Separation of AA Analytical separation Preparative separation Electrophoresis (based on charge) OC p
47 Ninhydrin test (AA is purple) 47
48 Paper Chromatograhpy and Thin-Layer Chromatography (based on polarity) Solvent: H 2 O/AcOH/BuOH MIT Chemistry Laboratory Techniques 48
49 Ion-Exchange Chromatography Cation-exchange resin Nonpolar nature of the column caused it to retain nonpolar amino acids longer than polar amino acids. Water softener OC p
50 50
51 51
52 After addition of ninhydrin At 570 nm 52
53 Synthesis of Amino acids Hell-Volhard-Zelinski reaction 53
54 54
55 Higher yield 55
56 56
57 Strecker synthesis 57
58 Kinetic resolution In kinetic resolution, two enantiomers show different reaction rates in a chemical reaction, thereby creating an excess of the less reactive enantiomer. This excess goes through a maximum and disappears on full completion of the reaction. Kinetic resolution is a very old concept in organic chemistry and can be used in the organic synthesis of chiral molecules. It has been surpassed by other methods. 58
59 4.7 What is the Fundamental Structural Pattern in Proteins? Proteins are unbranched polymers of amino acids Amino acids join head-to-tail through formation of covalent peptide bonds Peptide bond formation results in release of water The peptide backbone of a protein consists of the repeated sequence N-C α -C o - N is the amide nitrogen of the amino acid C α is the alpha-c of the amino acid C o is the carbonyl carbon of the amino acid
60 peptide bond (amide bond) 60
61 61
62 The Peptide Bond Is usually found in the trans conformation Has partial (40%) double bond character Is about nm long - shorter than a typical single bond but longer than a double bond Due to the double bond character, the six atoms of the peptide bond group are always planar N partially positive; O partially negative
63 40% double-bond character 63
64 4.7 What is the Fundamental Structural Pattern in Proteins? Figure 4.16 (c) The peptide bond is best described as a resonance hybrid of the forms shown on the two previous slides.
65 The Peptide Bond Figure 4.15 The trans conformation of the peptide bond.
66 4.7 What is the Fundamental Structural Pattern in Proteins? The coplanar relationship of the atoms in the amide group is highlighted here by an imaginary shaded plane lying between adjacent α-carbons.
67 67
68 Br 2 (or I 2 ) 68
69 69
70 70
71 71
72 72
73 Peptides Short polymers of amino acids Each unit is called a residue 2 residues - dipeptide 3 residues - tripeptide residues - oligopeptide many - polypeptide
74 Protein One or more polypeptide chains One polypeptide chain - a monomeric protein More than one - multimeric protein Homomultimer - one kind of chain Heteromultimer - two or more different chains Hemoglobin, for example, is a heterotetramer It has two alpha chains and two beta chains
75 75
76 Enkephalins synthesized by the body to control pain morphine 76
77 Peptide hormones Bradykinin inhibits the inflammation of tissues Vasopressin controls blood pressure Oxyocin induces labor in pregnant women by stimulating the uterine muscle 77
78 200 times sweeter than sucrose D-amino acid is bitter. 78
79 Destroy harmful oxidizing agents in the body 79
80 The Sequence of Amino Acids in a Protein Is a unique characteristic of every protein Is encoded by the nucleotide sequence of DNA Is thus a form of genetic information Is read from the amino terminus to the carboxyl terminus
81 Chemical Synthesis of peptide 81
82 Solid Phase Synthesis of Peptides R. Bruce Merrifield and his collaborators pioneered the solid-phase synthesis of polypeptides in the laboratory Carboxy terminus of a nascent peptide is covalently anchored to an insoluble resin After each addition of a residue, the resin particles are collected by filtration Automation and computer control now permit synthesis of peptides of 30 residues or more
83 83
84 Boc 84
85 85
86 86
87 87
88 88
89 89
90 90
91 91
92 92
93 Automated solid-phase peptide synthesis 93
94 94
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